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  • CCDC151 mutations cause primary ciliary dyskinesia by disruption of the outer dynein arm docking complex formation.

CCDC151 mutations cause primary ciliary dyskinesia by disruption of the outer dynein arm docking complex formation.

American journal of human genetics (2014-09-06)
Rim Hjeij, Alexandros Onoufriadis, Christopher M Watson, Christopher E Slagle, Nikolai T Klena, Gerard W Dougherty, Małgorzata Kurkowiak, Niki T Loges, Christine P Diggle, Nicholas F C Morante, George C Gabriel, Kristi L Lemke, You Li, Petra Pennekamp, Tabea Menchen, Franziska Konert, June Kehlet Marthin, Dorus A Mans, Stef J F Letteboer, Claudius Werner, Thomas Burgoyne, Cordula Westermann, Andrew Rutman, Ian M Carr, Christopher O'Callaghan, Eduardo Moya, Eddie M K Chung, Eamonn Sheridan, Kim G Nielsen, Ronald Roepman, Kerstin Bartscherer, Rebecca D Burdine, Cecilia W Lo, Heymut Omran, Hannah M Mitchison
ABSTRACT

A diverse family of cytoskeletal dynein motors powers various cellular transport systems, including axonemal dyneins generating the force for ciliary and flagellar beating essential to movement of extracellular fluids and of cells through fluid. Multisubunit outer dynein arm (ODA) motor complexes, produced and preassembled in the cytosol, are transported to the ciliary or flagellar compartment and anchored into the axonemal microtubular scaffold via the ODA docking complex (ODA-DC) system. In humans, defects in ODA assembly are the major cause of primary ciliary dyskinesia (PCD), an inherited disorder of ciliary and flagellar dysmotility characterized by chronic upper and lower respiratory infections and defects in laterality. Here, by combined high-throughput mapping and sequencing, we identified CCDC151 loss-of-function mutations in five affected individuals from three independent families whose cilia showed a complete loss of ODAs and severely impaired ciliary beating. Consistent with the laterality defects observed in these individuals, we found Ccdc151 expressed in vertebrate left-right organizers. Homozygous zebrafish ccdc151(ts272a) and mouse Ccdc151(Snbl) mutants display a spectrum of situs defects associated with complex heart defects. We demonstrate that CCDC151 encodes an axonemal coiled coil protein, mutations in which abolish assembly of CCDC151 into respiratory cilia and cause a failure in axonemal assembly of the ODA component DNAH5 and the ODA-DC-associated components CCDC114 and ARMC4. CCDC151-deficient zebrafish, planaria, and mice also display ciliary dysmotility accompanied by ODA loss. Furthermore, CCDC151 coimmunoprecipitates CCDC114 and thus appears to be a highly evolutionarily conserved ODA-DC-related protein involved in mediating assembly of both ODAs and their axonemal docking machinery onto ciliary microtubules.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Anti-CCDC114 antibody produced in rabbit, Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution
Sigma-Aldrich
Anti-Acetylated Tubulin antibody, Mouse monoclonal, clone 6-11B-1, purified from hybridoma cell culture
Sigma-Aldrich
Anti-ARMC4 antibody produced in rabbit, Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution
Sigma-Aldrich
GeneJuice® Transfection Reagent, Non-lipid based chemical transfection reagent optimized for maximum transfection efficiency, ease-of-use, and minimal cytotoxicity on a wide variety of mammalian cells.